ID A0A0A7KHK9_9DEIO Unreviewed; 318 AA.
AC A0A0A7KHK9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=GDP-L-fucose synthase {ECO:0000256|HAMAP-Rule:MF_00956};
DE EC=1.1.1.271 {ECO:0000256|HAMAP-Rule:MF_00956};
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase {ECO:0000256|HAMAP-Rule:MF_00956};
GN Name=fcl {ECO:0000256|HAMAP-Rule:MF_00956};
GN ORFNames=QR90_01180 {ECO:0000313|EMBL:AIZ44033.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ44033.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-
CC dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a
CC reductase reaction. {ECO:0000256|HAMAP-Rule:MF_00956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose +
CC H(+) + NADPH; Xref=Rhea:RHEA:18885, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58349; EC=1.1.1.271; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00956};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
CC {ECO:0000256|HAMAP-Rule:MF_00956}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Fucose synthase subfamily. {ECO:0000256|ARBA:ARBA00005959,
CC ECO:0000256|HAMAP-Rule:MF_00956}.
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DR EMBL; CP010028; AIZ44033.1; -; Genomic_DNA.
DR RefSeq; WP_039681667.1; NZ_CP010028.1.
DR AlphaFoldDB; A0A0A7KHK9; -.
DR STRING; 1182571.QR90_01180; -.
DR KEGG; dsw:QR90_01180; -.
DR HOGENOM; CLU_007383_18_0_0; -.
DR UniPathway; UPA00128; UER00191.
DR Proteomes; UP000030634; Chromosome.
DR GO; GO:0050577; F:GDP-L-fucose synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd05239; GDP_FS_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR HAMAP; MF_00956; GDP_fucose_synth; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR028614; GDP_fucose/colitose_synth.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43238; GDP-L-FUCOSE SYNTHASE; 1.
DR PANTHER; PTHR43238:SF1; GDP-L-FUCOSE SYNTHASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00956};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00956};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00956};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00956}; Reference proteome {ECO:0000313|Proteomes:UP000030634}.
FT DOMAIN 7..238
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 11..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 106..109
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 164..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00956"
SQ SEQUENCE 318 AA; 34483 MW; 18D94C4F0680CC42 CRC64;
MRLTDRIYVA GHGGLVGSAL LRRLKADGYS NVLTCSSREL DLRDQGAALA FFETERPQYV
FLAAAKVGGI HANSTRPAEF LYDNLMIAAN VIHAAHVTGV EKLLNLGSTC IYPRDAAQPL
REDALLTGPL EDTNRAYAVA KIAAIELCDQ YRAQYGDDFV SAMPTNLYGP GDNFDLMGSH
VLPALIRKMV DAREAGAPTV SVWGSGTPLR EFLHVDDLAD ACLFLMKNVS EPGPINVGTG
QDLSIREVAE QIRAVVGYTG ELAFDASKPD GTPRKITDVS RIHALGWHHR IALDEGLRST
VEWYLAHRGQ VRGEAVAG
//
